Application of maximum-entropy maps in the accurate refinement of a putative acylphosphatase using 1.3 Å X-ray diffraction data

Acta Crystallographica Section D: Biological Crystallography

Volumn 64, Issue 3, 2008, Pages 237-247

  Nishibori, Eiji ^a   Nakamura, Takahiro ^a   Arimoto, Masanori ^a   Aoyagi, Shinobu ^a   Ago, Hideo ^b   Miyano, Masashi ^b   Ebisuzaki, Toshikazu ^c   Sakata, Makoto ^a  

^a NAGOYA UNIVERSITY   (Japan)

^b RIKEN Harima Institute Research   (Japan)

^c RIKEN   (Japan)

Author keywords

High resolution structural refinement; Maximum entropy method; Near atomic resolution data

Indexed keywords

ACID ANHYDRIDE HYDROLASE; ACYLPHOSPHATASE;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER PROGRAM; ENTROPY; METHODOLOGY; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

ACID ANHYDRIDE HYDROLASES; CRYSTALLOGRAPHY, X-RAY; ENTROPY; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SOFTWARE; X-RAY DIFFRACTION;

EID: 40449138562     PISSN: 09074449     EISSN: 13990047     Source Type: Journal    
DOI: 10.1107/S0907444907065663     Document Type: Article

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